Biochemical evidences for M1-, M17- and M18-like aminopeptidases in marine invertebrates from Cuban coastline

Abstract

<jats:title>Abstract</jats:title><jats:p>Metallo-aminopeptidases (mAPs) control many physiological processes. They are classified in different families according to structural similarities. Neutral mAPs catalyze the cleavage of neutral amino acids from the N-terminus of proteins or peptide substrates; they need one or two metallic cofactors in their active site. Information about marine invertebrate’s neutral mAPs properties is scarce; available data are mainly derived from genomics and cDNA studies. The goal of this work was to characterize the biochemical properties of the neutral APs activities in eight Cuban marine invertebrate species from the Phyla Mollusca, Porifera, Echinodermata, and Cnidaria. Determination of substrate specificity, optimal pH and effects of inhibitors (1,10-phenanthroline, amastatin, and bestatin) and cobalt on activity led to the identification of distinct neutral AP-like activities, whose biochemical behaviors were similar to those of the M1 and M17 families of mAPs. Additionally, M18-like glutamyl AP activities were detected. Thus, marine invertebrates express biochemical activities likely belonging to various families of metallo-aminopeptidases.</jats:p>

Marine Invertebrates: A Promissory Still Unexplored Source of Inhibitors of Biomedically Relevant Metallo Aminopeptidases Belonging to the M1 and M17 Families

“…Marine organisms are an abundant source of bioactive molecules (including saccharides, polysaccharides, peptides, proteins, polyketides, polyphenolic compounds, sterol-like products, alkaloids, quinones, and quinolones, among others), such as toxins [ 20 , 21 ], antimicrobial peptides [ 22 , 23 ], antiviral compounds [ 24 ], enzymes and enzyme inhibitors [ 25 , 26 , 27 , 28 ], and particularly peptidases [ 29 , 30 ] and peptidase inhibitors of almost all mechanistic classes [ 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 ]. These bioactive molecules have a great diversity of chemical structures, high potency, and diverse specificities, especially the inhibitors of metalloenzymes ( Figure 2 , Figure 3 and Figure 4 ) [ 37 , 43 , 44 , 45 , 46 , 47 , 48 , 49 , 50 , 51 , 52 , 53 , 54 ]. These inhibitory biomolecules are frequently involved in nutrition, homeostasis, reproduction, and communication of marine organisms [ 27 ].…”